Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1KCG

NKG2D in complex with ULBP3

1KCG の概要
エントリーDOI10.2210/pdb1kcg/pdb
分子名称NKG2-D type II integral membrane protein, UL16-binding protein 3 (3 entities in total)
機能のキーワードprotein-protein complex, c-type lectin-like receptor, mhc class i-like molecule, immune system
由来する生物種Homo sapiens (human)
詳細
細胞内の位置Membrane; Single-pass type II membrane protein: P26718
Cell membrane; Lipid-anchor, GPI-anchor: Q9BZM4
タンパク質・核酸の鎖数3
化学式量合計50160.87
構造登録者
Radaev, S.,Sun, P. (登録日: 2001-11-08, 公開日: 2002-01-09, 最終更新日: 2024-12-25)
主引用文献Radaev, S.,Rostro, B.,Brooks, A.G.,Colonna, M.,Sun, P.D.
Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3.
Immunity, 15:1039-1049, 2001
Cited by
PubMed Abstract: NKG2D is known to trigger the natural killer (NK) cell lysis of various tumor and virally infected cells. In the NKG2D/ULBP3 complex, the structure of ULBP3 resembles the alpha1 and alpha2 domains of classical MHC molecules without a bound peptide. The lack of alpha3 and beta2m domains is compensated by replacing two hydrophobic patches at the underside of the class I MHC-like beta sheet floor with a group of hydrophilic and charged residues in ULBP3. NKG2D binds diagonally across the ULBP3 alpha helices, creating a complementary interface, an asymmetrical subunit orientation, and local conformational adjustments in the receptor. The interface is stabilized primarily by hydrogen bonds and hydrophobic interactions. Unlike the KIR receptors that recognize a conserved HLA region by a lock-and-key mechanism, NKG2D recognizes diverse ligands by an induced-fit mechanism.
PubMed: 11754823
DOI: 10.1016/S1074-7613(01)00241-2
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.6 Å)
構造検証レポート
Validation report summary of 1kcg
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

PDB statisticsPDBj update infoContact PDBjnumon